Title | Characterizing weak protein-protein complexes by NMR residual dipolar couplings. |
Publication Type | Journal Article |
Year of Publication | 2011 |
Authors | Ringkjøbing Jensen, M., J-L. Ortega-Roldan, L. Salmon, N. A. J. van Nuland, and M. Blackledge |
Journal | Eur Biophys J |
Volume | 40 |
Issue | 12 |
Pagination | 1371-81 |
Date Published | 2011 Dec |
ISSN | 1432-1017 |
Keywords | Macromolecular Substances, Magnetic Resonance Spectroscopy, Molecular Dynamics Simulation, Protein Binding, Protein Structure, Tertiary, Proteins |
Abstract | Protein-protein interactions occur with a wide range of affinities from tight complexes characterized by femtomolar dissociation constants to weak, and more transient, complexes of millimolar affinity. Many of the weak and transiently formed protein-protein complexes have escaped characterization due to the difficulties in obtaining experimental parameters that report on the complexes alone without contributions from the unbound, free proteins. Here, we review recent developments for characterizing the structures of weak protein-protein complexes using nuclear magnetic resonance spectroscopy with special emphasis on the utility of residual dipolar couplings. |
DOI | 10.1007/s00249-011-0720-5 |
Alternate Journal | Eur. Biophys. J. |
PubMed ID | 21710303 |
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